Reviewed, UniProtKB/Swiss-Prot Q0UZK0 (KYNU2_PHANO)

Names and origin

Protein names

Recommended name:
    Kynureninase 2
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase 2
    Biosynthesis of nicotinic acid protein 5-2

Gene names

Name:	BNA5-2
ORF Names:	SNOG_02814

Organism

Phaeosphaeria nodorum (Glume blotch fungus) (Septoria nodorum) [Complete proteome]

Taxonomic identifier

13684 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Pleosporomycetidae › Pleosporales › Phaeosphaeriaceae › Phaeosphaeria

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively By similarity.
Catalytic activity	L-kynurenine + H2O = anthranilate + L-alanine. L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the kynureninase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from electronic annotation. Source: InterPro tryptophan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kynureninase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 489	489	Kynureninase 2		PRO_0000356983
Regions
	Region	177 – 180	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	149	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	150	1	Pyridoxal phosphate By similarity
	Binding site	261	1	Pyridoxal phosphate By similarity
	Binding site	264	1	Pyridoxal phosphate By similarity
	Binding site	286	1	Pyridoxal phosphate By similarity
	Binding site	317	1	Pyridoxal phosphate By similarity
	Binding site	345	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	287	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0UZK0-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 4F2FBB290F1825BE	FASTA	489	54,097
	10 20 30 40 50 60 MDASAAISQL RQGQKPEWPQ NANTSDFAKT LDNSSEFPKT LRHEYVVPTK AQLKRKTLND 70 80 90 100 110 120 DAQTAAKASS SDDEGIYFCG NSLGLQPKAV GEYLNAYLKT WGSIAVGSHF TPMADSPLTP 130 140 150 160 170 180 FQDMAAECAR RMSDIVGASP SEIVAMNTLT INLHLMMAAF YKPTEKKHKI MCEWRPFPSD 190 200 210 220 230 240 WYAIESQIEW HGLDPKKSML LVKPDDGYLM TTESILKLID QEADELALIM LPGIQYYSGQ 250 260 270 280 290 300 LLDIPTITTH ARKHGITIGW DLAHAAGNVE LKLHDWDVDF ACWCTYKYMN AGAGAIAGAF 310 320 330 340 350 360 VHSKHGDNGS NVGLKGWYGH DKSSRFLMDN KFVPTPGAQG FQCSNPSAVD LTCLAGSLSV 370 380 390 400 410 420 FQKTSVADLR SRSLLLTAYA EHLLTQIASR NIKDGNFPFQ IISPLDPRFR GAQLSVLLQE 430 440 450 460 470 480 DVMEEVFAGL EENGVICDKR KPGIIRVAPV PMYNTFEDVY KFMHILEGAL QPKAEQKTQA HGEAVEARL

References

[1]

"Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum." Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P. Plant Cell 19:3347-3368(2007) [PubMed: 18024570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SN15.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH445328 Genomic DNA. Translation: EAT89545.1.
RefSeq	XP_001793409.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5970266.
Phylogenomic databases
OMA	WQPLSGW.
Family and domain databases
InterPro	IPR010111. Kynureninase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR14084. Kynureninase. 1 hit.
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU2_PHANO

Accession

Primary (citable) accession number: Q0UZK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	September 5, 2006
Last modified:	November 3, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)